A single amino acid mutation of ala-773 in the mineralocorticoid receptor confers agonist properties to 11beta-substituted spirolactones.

@article{Auzou2000ASA,
  title={A single amino acid mutation of ala-773 in the mineralocorticoid receptor confers agonist properties to 11beta-substituted spirolactones.},
  author={Gilles Auzou and J{\'e}r{\^o}me Fagart and Anny Souque and CHANTAL HELLAL-L{\'E}VY and J M Wurtz and Dino Moras and Marie-Edith Rafestin-Oblin},
  journal={Molecular pharmacology},
  year={2000},
  volume={58 4},
  pages={684-91}
}
Sequence analysis revealed a strong homology between the ligand-binding domain (LBD) of the human mineralocorticoid receptor (hMR) and glucocorticoid receptor (hGR). Nevertheless, steroids with bulky C11-substituents bind to hGR, unlike hMR. In this report, a mutant hMR, in which the residue Ala-773 facing the C11 steroid position was replaced by a glycine (A773G), was assayed for its capacity to bind steroids, to interact with receptor coactivators, and to stimulate transcription. The capacity… CONTINUE READING

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